Purification and some properties of buffalo spleen cathepsin Β.
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Date
1989-09
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Abstract
Purification of cathepsin Β from buffalo-spleen, a hitherto unstudied system has
been achieved by a simple procedure developed by incorporating suitable modifications in
the existing methods for isolation of the enzyme from other sources. The purified enzyme
has a molecular weight of 25 KDa and its Stokes radius was found to be 2·24 nm. Effects
of several reducing agents, urea and thiol-protease inhibitors such as leupeptin and antipain,
have been studied and the data unequivocally support the contention that the buffaloenzyme
is similar to cathepsin Β from other tissues with respect to these properties.
Description
Keywords
Lysosomal proteases, cathepsin Β, buffalo-spleen, hydrodynamic properties
Citation
Ahmad Sarfraz, Agarwal Sudhir K, Khan M Yahiya. Transplantation of fetal neocortex in rhesus monkey. Journal of Biosciences. 1989 Sep; 14(3): 261-268.